Alkaline solutions of a mixture from rapeseed globulin and casein show plastic flow, which is influenced by protein concentration, relation of rapeseed globulin and casein, temperature and time of storage of the protein solution. The sodium hydroxide concentration with a great variability doesn't take effect on the rheological properties. With increasing content of casein in such alkaline solutions of rapeseed globuline and casein results an approach to NEWTONian flow. The spinnability of alkaline solutions of a mixture from rapeseed globulin and casein and the properties of the corresponding spun protein fibers are influenced by protein concentration, relation of rapeseed globulin and casein of the spinning solution and temperature of coagulating bath. The sodium hydroxide content of the spinning solution and the hydrochloric acid concentration of the coagulating bath with a great variability don't take effect. The spinnability of alkaline solutions of a mixture from rapeseed albumin starchsulphate and casein and the properties of the corresponding spun protein fibers compared to rapeseed globulin-casein mixtures are influenced additionally by sodium hydroxide concentration of the spinning solution and hydrochloric acid content of coagulating bath. The favourable influence on the properties of spun rapeseed albuminstarchsulphate-casein fibers isn't increased by a growth of the rapeseed albumin starchsulphate content more then 4% of the protein concentration of the spinning solution.
With spun protein fibers of casein and a mixture of casein and vegetable proteins results in a solution of sodium hydrogencarbonate an increased diameter of the protein fibers. The determination of this change makes possible an examination of the swellability and stability of the structure of protein fibers.
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